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Mutational analysis of protein folding pathways: the P22 tailspike endorhamnosidase.

作者信息

King J, Yu M H

出版信息

Methods Enzymol. 1986;131:250-66. doi: 10.1016/0076-6879(86)31044-9.

DOI:10.1016/0076-6879(86)31044-9
PMID:3773760
Abstract
摘要

相似文献

1
Mutational analysis of protein folding pathways: the P22 tailspike endorhamnosidase.
Methods Enzymol. 1986;131:250-66. doi: 10.1016/0076-6879(86)31044-9.
2
Properties of monoclonal antibodies selected for probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase.用于探测P22尾刺内鼠李糖苷酶野生型和突变型构象的单克隆抗体的特性。
J Biol Chem. 1990 Jun 25;265(18):10347-51.
3
Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase.热稳定的P22尾刺内鼠李糖苷酶的热解折叠途径。
Biochemistry. 1991 Jun 25;30(25):6260-9. doi: 10.1021/bi00239a026.
4
Genetic and biochemical analysis of in vivo protein folding and subunit assembly.体内蛋白质折叠和亚基组装的遗传与生化分析。
Biopolymers. 1983 Jan;22(1):125-9. doi: 10.1002/bip.360220120.
5
Characterization of bacteriophage P22 tailspike mutant proteins with altered endorhamnosidase and capsid assembly activities.
J Biol Chem. 1989 Nov 25;264(33):20112-9.
6
Single amino acid substitutions influencing the folding pathway of the phage P22 tail spike endorhamnosidase.影响噬菌体P22尾刺内鼠李糖苷酶折叠途径的单氨基酸取代
Proc Natl Acad Sci U S A. 1984 Nov;81(21):6584-8. doi: 10.1073/pnas.81.21.6584.
7
Smooth specific phage adsorption: endorhamnosidase activity of tail parts of P22.平滑的特异性噬菌体吸附：P22尾部的内鼠李糖苷酶活性
Biochem Biophys Res Commun. 1973 Nov 16;55(2):403-9. doi: 10.1016/0006-291x(73)91101-7.
8
Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein. III. Intensive polypeptide chains synthesized at 39 degrees C.在噬菌体P22尾刺蛋白折叠或亚基组装过程中受阻的温度敏感突变体。III. 在39摄氏度下合成的密集多肽链。
J Mol Biol. 1981 Feb 5;145(4):653-76. doi: 10.1016/0022-2836(81)90308-9.
9
Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase.噬菌体P22尾刺内鼠李糖苷酶平行β-螺旋结构域中温度敏感折叠突变的发生率。
J Mol Biol. 1997 Mar 21;267(1):88-102. doi: 10.1006/jmbi.1996.0841.
10
Secondary structure and thermostability of the phage P22 tailspike. XX. Analysis by Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant.
J Mol Biol. 1988 Feb 5;199(3):491-502. doi: 10.1016/0022-2836(88)90620-1.

引用本文的文献

1
Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state.与它们在蛋白质中的定位无关，疏水性氨基酸残基对去辅基肌红蛋白的无定形球蛋白状态没有影响，而去辅基肌红蛋白表面的二硫键稳定了这种中间状态。
PLoS One. 2014 Jun 3;9(6):e98645. doi: 10.1371/journal.pone.0098645. eCollection 2014.
2
Kinetic folding studies of the P22 tailspike beta-helix domain reveal multiple unfolded states.P22尾刺β-螺旋结构域的动力学折叠研究揭示了多种未折叠状态。
Biophys Chem. 2009 May;141(2-3):214-21. doi: 10.1016/j.bpc.2009.02.001. Epub 2009 Feb 12.
3
Three amino acids that are critical to formation and stability of the P22 tailspike trimer.
对P22尾刺三聚体的形成和稳定性至关重要的三种氨基酸。
Protein Sci. 2005 Sep;14(9):2333-43. doi: 10.1110/ps.051394605. Epub 2005 Aug 4.
4
Pressure dissociation studies provide insight into oligomerization competence of temperature-sensitive folding mutants of P22 tailspike.压力解离研究为了解P22尾刺温度敏感折叠突变体的寡聚化能力提供了线索。
Protein Sci. 2004 Jun;13(6):1538-46. doi: 10.1110/ps.03579304. Epub 2004 May 7.
5
C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.C 末端疏水相互作用在 P22 尾刺三聚体的寡聚组装中起关键作用。
Protein Sci. 2003 Dec;12(12):2732-47. doi: 10.1110/ps.03150303.
6
Nonnative interactions between cysteines direct productive assembly of P22 tailspike protein.半胱氨酸之间的非天然相互作用指导P22尾刺蛋白的有效组装。
Biophys J. 2003 Nov;85(5):3237-47. doi: 10.1016/S0006-3495(03)74741-9.
7
Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation.在有效折叠与非天然聚集交界处对热不稳定尾刺中间体进行低温挽救。
Protein Sci. 1998 Jul;7(7):1516-23. doi: 10.1002/pro.5560070704.
8
Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies.用单克隆抗体探测P22尾刺折叠和聚集中间体的构象
Protein Sci. 1997 Jan;6(1):99-108. doi: 10.1002/pro.5560060111.
9
Protein engineering. The design, synthesis and characterization of factitious proteins.蛋白质工程。人工合成蛋白质的设计、合成与表征。
Biochem J. 1987 Aug 15;246(1):1-17. doi: 10.1042/bj2460001.
10
Identification of sites influencing the folding and subunit assembly of the P22 tailspike polypeptide chain using nonsense mutations.利用无义突变鉴定影响P22尾刺多肽链折叠和亚基组装的位点。
Genetics. 1987 Oct;117(2):157-71. doi: 10.1093/genetics/117.2.157.